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Two functionally distinct HEATR5 protein complexes are defined by fast-evolving co-factors in yeast.

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Budding yeast Laa1 protein functions in two distinct complexes, revealing how HEATR5 proteins bind co-factors. These findings uncover Laa1

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Structural Biology

Background:

  • HEATR5 proteins are crucial for membrane traffic, interacting with adaptor protein complex-1 (AP1).
  • The precise mechanisms by which HEATR5 proteins engage their rapidly evolving co-factors remain largely unelucidated.

Approach:

  • Investigated the budding yeast HEATR5 protein, Laa1, utilizing biochemical analyses and structure predictions.
  • Identified two distinct Laa1-containing complexes, differentiated by mutually exclusive binding partners Laa2 and Lft1.
  • Examined the structural basis of Lft1 and Laa2 interactions with Laa1, despite limited sequence homology.

Key Points:

  • Laa1 operates within two biochemically distinct complexes, involving Laa2 and the novel protein Lft1.
  • Both Laa1 complexes are implicated in intra-Golgi recycling pathways.
  • Only the Laa2-Laa1 complex demonstrates direct binding to AP1, influencing its cellular localization.

Conclusions:

  • Elucidated a conserved, structurally similar mechanism for HEATR5 co-factor binding in yeast and humans.
  • Demonstrated that Laa1 possesses functions beyond AP1 recruitment, expanding our understanding of its cellular roles.
  • Provided mechanistic insights into HEATR5 protein interactions and their implications in membrane trafficking.